BCD1_YEAST
ID BCD1_YEAST Reviewed; 366 AA.
AC P38772; D3DKY8;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Box C/D snoRNA protein 1;
GN Name=BCD1; OrderedLocusNames=YHR040W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP FUNCTION.
RX PubMed=12837249; DOI=10.1016/s0092-8674(03)00466-5;
RA Peng W.-T., Robinson M.D., Mnaimneh S., Krogan N.J., Cagney G.,
RA Morris Q.D., Davierwala A.P., Grigull J., Yang X., Zhang W., Mitsakakis N.,
RA Ryan O.W., Datta N., Jojic V., Pal C., Canadien V., Richards D.P.,
RA Beattie B., Wu L.F., Altschuler S.J., Roweis S., Frey B.J., Emili A.,
RA Greenblatt J.F., Hughes T.R.;
RT "A panoramic view of yeast noncoding RNA processing.";
RL Cell 113:919-933(2003).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
RA Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M.,
RA Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E.,
RA Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.;
RT "Assigning function to yeast proteins by integration of technologies.";
RL Mol. Cell 12:1353-1365(2003).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-330, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
CC -!- FUNCTION: Required for box C/D snoRNAs accumulation involved in snoRNA
CC processing, snoRNA transport to the nucleolus and ribosome biogenesis.
CC {ECO:0000269|PubMed:12837249}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:14690591}.
CC -!- MISCELLANEOUS: Present with 2800 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the BCD1 family. {ECO:0000305}.
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DR EMBL; U00062; AAB68905.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06732.1; -; Genomic_DNA.
DR PIR; S46736; S46736.
DR RefSeq; NP_011906.1; NM_001179170.1.
DR PDB; 2N94; NMR; -; A=1-45.
DR PDB; 6NZ2; NMR; -; A=120-303.
DR PDB; 6THL; X-ray; 2.80 A; B=120-303.
DR PDBsum; 2N94; -.
DR PDBsum; 6NZ2; -.
DR PDBsum; 6THL; -.
DR AlphaFoldDB; P38772; -.
DR SMR; P38772; -.
DR BioGRID; 36472; 211.
DR DIP; DIP-3862N; -.
DR IntAct; P38772; 7.
DR STRING; 4932.YHR040W; -.
DR iPTMnet; P38772; -.
DR MaxQB; P38772; -.
DR PaxDb; P38772; -.
DR PRIDE; P38772; -.
DR EnsemblFungi; YHR040W_mRNA; YHR040W; YHR040W.
DR GeneID; 856436; -.
DR KEGG; sce:YHR040W; -.
DR SGD; S000001082; BCD1.
DR VEuPathDB; FungiDB:YHR040W; -.
DR eggNOG; KOG2858; Eukaryota.
DR GeneTree; ENSGT00390000017201; -.
DR HOGENOM; CLU_025524_3_0_1; -.
DR InParanoid; P38772; -.
DR OMA; QNKSKWD; -.
DR BioCyc; YEAST:G3O-31099-MON; -.
DR PRO; PR:P38772; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38772; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0070761; C:pre-snoRNP complex; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030515; F:snoRNA binding; IDA:SGD.
DR GO; GO:0000492; P:box C/D snoRNP assembly; IDA:SGD.
DR GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR GO; GO:0042254; P:ribosome biogenesis; IDA:SGD.
DR GO; GO:0016074; P:sno(s)RNA metabolic process; IMP:SGD.
DR GO; GO:0048254; P:snoRNA localization; IBA:GO_Central.
DR InterPro; IPR007529; Znf_HIT.
DR Pfam; PF04438; zf-HIT; 1.
DR PROSITE; PS51083; ZF_HIT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Ribosome biogenesis; Zinc; Zinc-finger.
FT CHAIN 1..366
FT /note="Box C/D snoRNA protein 1"
FT /id="PRO_0000173558"
FT ZN_FING 5..39
FT /note="HIT-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT REGION 318..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 5
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT BINDING 8
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT BINDING 17
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT BINDING 20
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT BINDING 25
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT BINDING 29
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT BINDING 33
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT BINDING 39
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00453"
FT MOD_RES 330
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT STRAND 6..8
FT /evidence="ECO:0007829|PDB:2N94"
FT TURN 18..20
FT /evidence="ECO:0007829|PDB:2N94"
FT HELIX 27..37
FT /evidence="ECO:0007829|PDB:2N94"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:2N94"
FT STRAND 127..130
FT /evidence="ECO:0007829|PDB:6NZ2"
FT STRAND 133..136
FT /evidence="ECO:0007829|PDB:6THL"
FT HELIX 143..147
FT /evidence="ECO:0007829|PDB:6THL"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:6THL"
FT TURN 154..157
FT /evidence="ECO:0007829|PDB:6THL"
FT STRAND 158..167
FT /evidence="ECO:0007829|PDB:6THL"
FT STRAND 180..191
FT /evidence="ECO:0007829|PDB:6THL"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:6THL"
FT HELIX 199..208
FT /evidence="ECO:0007829|PDB:6THL"
FT TURN 218..220
FT /evidence="ECO:0007829|PDB:6NZ2"
FT HELIX 227..235
FT /evidence="ECO:0007829|PDB:6THL"
FT STRAND 240..244
FT /evidence="ECO:0007829|PDB:6THL"
FT STRAND 258..261
FT /evidence="ECO:0007829|PDB:6THL"
FT HELIX 264..266
FT /evidence="ECO:0007829|PDB:6THL"
FT HELIX 269..273
FT /evidence="ECO:0007829|PDB:6THL"
FT STRAND 277..281
FT /evidence="ECO:0007829|PDB:6THL"
FT STRAND 283..290
FT /evidence="ECO:0007829|PDB:6THL"
SQ SEQUENCE 366 AA; 42334 MW; EE8BDAF489EC1F12 CRC64;
MAVLCGVCGI KEFKYKCPRC LVQTCSLECS KKHKTRDNCS GQTHDPKEYI SSEALKQADD
DKHERNAYVQ RDYNYLTQLK RMVHVQKMDA RMKNKRVLGP VGGHNSNFKK RRYDIDEDDR
DSTECQRIIR RGVNCLMLPK GMQRSSQNRS KWDKTMDLFV WSVEWILCPM QEKGEKKELF
KHVSHRIKET DFLVQGMGKN VFQKCCEFYR LAGTSSCIEG EDGSETKEER TQILQKSGLK
FYTKTFPYNT THIMDSKKLV ELAIHEKCIG ELLKNTTVIE FPTIFVAMTE ADLPEGYEVL
HQEPRPLEHT STLNKFIDNA REEEDAEEDS QPTEEPVQKE TQDASDSDSD SDDDYNPGLS
MDFLTA
